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(Journal Article): Glucagon-like peptide 1(7-36)amide: characterization of the domain responsible for binding to its receptor on rat insulinoma RINm5F cells.
Gallwitz B, Schmidt WE, Conlon JM, Creutzfeldt W (Division of Gastroenterology and Endocrinology, Georg August University, Gottingen, Federal Republic of Germany.)
IN:
J Mol Endocrinol
1990; 5:33-39
Impact Factor(s) of J Mol Endocrinol: 3.855 (2004), 3.701 (2003), 4.359 (2002), 3.649 (2001)
ABSTRACT: Glucagon-like peptide-1(7-36)amide (GLP-1(7-36)amide) is a potent stimulator of insulin secretion. Receptors for this hormone have been found on different insulinoma-derived cell lines, e.g. the RINm5F cell line which is derived from a radiation-induced rat insulinoma. To characterize the part of the GLP-1(7-36)amide molecule that is responsible for binding to its receptor on RINm5F cells, binding studies with synthetic C-terminal (GLP-1(21-36)amide) and synthetic N-terminal (GLP-1(7-25] GLP-1 fragments were carried out. GLP-1(21-36)amide showed dose-dependent binding to the GLP-1(7-36)amide receptor but was approximately 1500 times less potent in inhibiting binding of 125I-labelled GLP-1(7-36)amide than the intact hormone. GLP-1(7-25) at concentrations up to 10 mumol/l did not inhibit binding of label. Neither fragment changed intracellular cyclic AMP concentrations, in contrast to GLP-1(7-36)amide which increased intracellular cyclic AMP. GLP-1(21-36)amide, however, acted as a weak partial antagonist of GLP-1(7-36)amide with respect to GLP-1(7-36)amide-dependent stimulation of cyclic AMP production.
TYPE OF PUBLICATION: Original article
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